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Calcium in PDB 1wyg: Crystal Structure of A Rat Xanthine Dehydrogenase Triple Mutant (C535A, C992R and C1324S)

Enzymatic activity of Crystal Structure of A Rat Xanthine Dehydrogenase Triple Mutant (C535A, C992R and C1324S)

All present enzymatic activity of Crystal Structure of A Rat Xanthine Dehydrogenase Triple Mutant (C535A, C992R and C1324S):
1.1.1.204; 1.1.3.22;

Protein crystallography data

The structure of Crystal Structure of A Rat Xanthine Dehydrogenase Triple Mutant (C535A, C992R and C1324S), PDB code: 1wyg was solved by T.Nishino, K.Okamoto, Y.Kawaguchi, H.Hori, T.Matsumura, B.T.Eger, E.F.Pai, T.Nishino, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.00 / 2.60
Space group I 41 2 2
Cell size a, b, c (Å), α, β, γ (°) 134.253, 134.253, 523.315, 90.00, 90.00, 90.00
R / Rfree (%) 20.3 / 24.8

Other elements in 1wyg:

The structure of Crystal Structure of A Rat Xanthine Dehydrogenase Triple Mutant (C535A, C992R and C1324S) also contains other interesting chemical elements:

Iron (Fe) 4 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of A Rat Xanthine Dehydrogenase Triple Mutant (C535A, C992R and C1324S) (pdb code 1wyg). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Crystal Structure of A Rat Xanthine Dehydrogenase Triple Mutant (C535A, C992R and C1324S), PDB code: 1wyg:

Calcium binding site 1 out of 1 in 1wyg

Go back to Calcium Binding Sites List in 1wyg
Calcium binding site 1 out of 1 in the Crystal Structure of A Rat Xanthine Dehydrogenase Triple Mutant (C535A, C992R and C1324S)


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of A Rat Xanthine Dehydrogenase Triple Mutant (C535A, C992R and C1324S) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca4001

b:28.2
occ:1.00
 O A:THR870 2.6 21.8 1.0
OG A:SER874 2.6 33.6 1.0
O A:ASN908 2.6 21.4 1.0
OG A:SER907 2.7 21.1 1.0
O A:GLU871 2.9 24.3 1.0
O A:GLY867 3.0 35.5 1.0
CB A:ASP872 3.4 25.6 1.0
N A:ASN908 3.5 23.3 1.0
C A:GLU871 3.5 22.8 1.0
C A:ASN908 3.7 22.8 1.0
C A:THR870 3.7 21.2 1.0
C A:GLY867 3.8 33.4 1.0
CB A:SER907 3.9 22.6 1.0
CB A:SER874 3.9 31.4 1.0
C A:SER907 4.1 24.3 1.0
NE2 A:HIS840 4.1 35.9 1.0
CA A:ASN908 4.1 24.3 1.0
CA A:SER907 4.2 24.6 1.0
N A:ASP872 4.2 24.4 1.0
CA A:GLY867 4.3 34.1 1.0
CA A:GLU871 4.3 20.2 1.0
CE1 A:HIS840 4.4 37.1 1.0
CA A:ASP872 4.4 24.8 1.0
N A:SER874 4.5 31.9 1.0
N A:GLU871 4.5 20.5 1.0
CG A:ASP872 4.5 28.6 1.0
N A:THR870 4.7 23.8 1.0
CA A:SER874 4.7 31.8 1.0
CA A:THR870 4.7 21.3 1.0
N A:GLY868 4.8 32.5 1.0
CB A:ASN908 4.8 27.1 1.0
N A:LEU873 4.8 27.4 1.0
N A:THR909 4.8 23.1 1.0
C A:ASP872 4.9 25.3 1.0

Reference:

T.Nishino, K.Okamoto, Y.Kawaguchi, H.Hori, T.Matsumura, B.T.Eger, E.F.Pai, T.Nishino. Mechanism of the Conversion of Xanthine Dehydrogenase to Xanthine Oxidase: Identification of the Two Cysteine Disulfide Bonds and Crystal Structure of A Non-Convertible Rat Liver Xanthine Dehydrogenase Mutant J.Biol.Chem. V. 280 24888 2005.
ISSN: ISSN 0021-9258
PubMed: 15878860
DOI: 10.1074/JBC.M501830200
Page generated: Fri Jul 12 07:25:31 2024

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